Note. The novel sequence data published for Lep d I have been submitted to the EMBL data bank and are available under accession number X81399.
Primary Structure of Lep D I, the Main Lepidoglyphus Destructor Allergen
Article first published online: 3 MAR 2005
European Journal of Biochemistry
Volume 225, Issue 1, pages 93–98, October 1994
How to Cite
Varela, J., Ventas, P., Carreira, J., Barbas, J. A., Gimenez-Gallego, G. and Polo, F. (1994), Primary Structure of Lep D I, the Main Lepidoglyphus Destructor Allergen. European Journal of Biochemistry, 225: 93–98. doi: 10.1111/j.1432-1033.1994.00093.x
Supplementary Material. Primary structure of Lep d I, the main Lepidoglyphus destructor allergen. Fig. S1. Mass spectrometry of Lep d I. Fig. S2. Reverse-phase HPLC analysis of a tryptic digest of Lep d I. Fig. S3. Reverse-phase HPLC rechromatography of a chymotryptic digest of S -carboxymethylated Lep d I. Fig. S4. Reverse-phase HPLC analysis of a Staphylococcus aureus V8 digest of S -carboxymethylated Lep d I. Fig. S5. Reverse-phase HPLC analysis of an endoprotease Asp-N digest of S -carboxymethylated Lep d I. Fig. S6. Reverse-phase HPLC analysis of proline endopeptidase digest of peptide N-7. Fig. S7. Primers used to amplify by PCR a 3′ portion of cDNA of Lep d I. This information is available, upon request, from the Editorial Office. A total of 14 pages are available.
- Issue published online: 3 MAR 2005
- Article first published online: 3 MAR 2005
- (Received May 26/July 18, 1994) – EJB 94 0750/3
The most relevant allergen of the storage mite Lepidoglyphus destructor (Lep d I) has been characterized. Lep d I is a monomer protein of 13273 Da. The primary structure of Lep d I was determined by N-terminal Edman degradation and partially confirmed by cDNA sequencing. Sequence polymorphism was observed at six positions, with non-conservative substitutions in three of them. No potential N-glycosylation site was revealed by peptide sequencing, The 125-residue sequence of Lep d I shows approximately 40% identity (including the six cysteines) with the overlapping regions of group II allergens from the genus Dermatophagoides, which, however, do not share common allergenic epitopes with Lep d I.
radio allergosorbent test
rapid amplification of cDNA 3′ end
Trypsin (EC 184.108.40.206)
chymotrypsin (EC 220.127.116.11)
endoproteinase Glu-C (EC 18.104.22.168)
endoproteinase Asp-N (EC 22.214.171.124)
proline-specific endopeptidase (EC 126.96.36.199)
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